NDLI: Origin of Tryptophan Fluorescence Lifetimes. Part 2: Fluorescence Lifetimes Origin of Tryptophan in Proteins

Content Provider	Springer Nature Link
Author	Albani, J. R.
Copyright Year	2013
Abstract	Fluorescence intensity decays of L-tryptophan in proteins dissolved in pH 7 buffer, in ethanol and in 6 M guanidine pH 7.8 and in lyophilized proteins were measured. In all protein conditions, three lifetimes were obtained along the emission spectrum (310–410 nm). The two shortest lifetimes are in the same range of those obtained for L-Trp in water or in ethanol. Thus, these two lifetimes originate from specific two sub-structures existing in the excited state and are inherent to the tryptophan structure independently of the surrounding environment (amino acids residues, solvent, etc.) In proteins, the third lifetime originates from the interactions that are occurring between tryptophan residues and neighboring amino acids. Populations of these lifetimes are independent of the excitation wavelength and thus originate from pre-defined sub structures existing in the excited state and put into evidence after tryptophan excitation. Fluorescence decay studies of different tripeptides having a tryptophan residue in second position show that the best analysis is obtained with two fluorescence lifetimes. Consequently, this result seems to exclude the possibility that peptide bond induces the third fluorescence lifetimes. Indole dissolved in water and/or in ethanol emits with two fluorescence lifetimes that are completely different from those observed for L-Trp. Absence of the third lifetime in ethanol demonstrates that indole behaves differently when compared to tryptophan. Thus, it seems not adequate to attribute fluorescence lifetime or fluorescence properties of tryptophan to indole ring and to compare tryptophan fluorescence properties in proteins to molecules having close structures such as NATA which fluoresces with one lifetime.
Starting Page	105
Ending Page	117
Page Count	13
File Format	PDF
ISSN	10530509
Journal	Journal of Fluorescence
Volume Number	24
Issue Number	1
e-ISSN	15734994
Language	English
Publisher	Springer US
Publisher Date	2013-08-03
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Tryptophan Fluorescence lifetimes Lifetimes pre-exponentials Protein folding Tryptophan-amino acids interactions Sub-structures at the excitation state Biomedicine general Biophysics and Biological Physics Biotechnology Biochemistry Analytical Chemistry
Content Type	Text
Resource Type	Article
Subject	Sociology and Political Science Spectroscopy Law Biochemistry Clinical Biochemistry Clinical Psychology

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